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Open data
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Basic information
Entry | Database: PDB / ID: 1cfe | ||||||
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Title | P14A, NMR, 20 STRUCTURES | ||||||
![]() | PATHOGENESIS-RELATED PROTEIN P14A![]() | ||||||
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Function / homology | ![]() defense response to fungus / killing of cells of another organism / ![]() Similarity search - Function | ||||||
Biological species | ![]() ![]() ![]() | ||||||
Method | ![]() | ||||||
![]() | Fernandez, C. / Szyperski, T. / Bruyere, T. / Ramage, P. / Mosinger, E. / Wuthrich, K. | ||||||
![]() | ![]() Title: NMR solution structure of the pathogenesis-related protein P14a. Authors: Fernandez, C. / Szyperski, T. / Bruyere, T. / Ramage, P. / Mosinger, E. / Wuthrich, K. #1: ![]() Title: Pathogenesis-Related Pr-1 Proteins are Antifungal. Isolation and Characterization of Three 14-Kilodalton Proteins of Tomato and of a Basic Pr-1 of Tobacco with Inhibitory Activity Against Phytophthora Infestans Authors: Niderman, T. / Genetet, I. / Bruyere, T. / Gees, R. / Stintzi, A. / Legrand, M. / Fritig, B. / Mosinger, E. #2: ![]() Title: Amino Acid Sequence of the Pathogenesis-Related Leaf Protein P14 from Viroid-Infected Tomato Reveals a New Type of Structurally Unfamiliar Proteins Authors: Lucas, J. / Camacho Henriquez, A. / Lottspeich, F. / Henschen, A. / Sanger, H.L. | ||||||
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 875.2 KB | Display | ![]() |
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PDB format | ![]() | 767.2 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Arichive directory | ![]() ![]() | HTTPS FTP |
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-Related structure data
Similar structure data |
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Links
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Assembly
Deposited unit | ![]()
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NMR ensembles |
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Components
#1: Protein | ![]() Mass: 14914.463 Da / Num. of mol.: 1 / Fragment: RESIDUES 1 - 135 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() ![]() ![]() |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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NMR experiment | Type![]() |
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Sample preparation
Sample conditions | pH: 5.5 / Temperature: 303 K |
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Crystal grow![]() | *PLUS Method: other / Details: NMR |
-NMR measurement
NMR spectrometer |
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Processing
NMR software |
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Refinement | Method: distance geometry / Software ordinal: 1 | |||||||||
NMR ensemble | Conformer selection criteria: target function / Conformers calculated total number: 100 / Conformers submitted total number: 20 |